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Isolation of novel ACE‐inhibitory peptide from naked oat globulin hydrolysates in silico approach: Molecular docking, in vivo antihypertension and effects on renin and intracellular endothelin‐1
Author(s) -
Zheng Yajun,
Wang Xian,
Zhuang Yongliang,
Li Yan,
Shi Panqi,
Tian Hailong,
Li Xiaotian,
Chen Xing
Publication year - 2020
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/1750-3841.15115
Subject(s) - chemistry , captopril , hydrolysate , peptide , in vivo , renin–angiotensin system , chromatography , hydrolysis , biochemistry , blood pressure , endocrinology , biology , microbiology and biotechnology
Naked oat globulin was hydrolyzed by alcalase, flavourzyme, pepsin, and trypsin in sequence. The hydrolysates (NOGH) were purified using gel chromatography, reversed‐phase high performance liquid chromatography (RP‐HPLC). Finally, fraction D7d with the highest ACE‐inhibitory was subjected to liquid chromatography‐mass spectrometry analysis and 14 peptides were identified. Of which, peptide SSYYPFK (890.4 Da) was chose to synthesize based on in silico analysis. The SSYYPFK demonstrated high ACE‐inhibitory activity (IC 50 : 91.82 µM) with competitive inhibition mode, and could effectively ( P < 0.05) lower the systolic blood pressure and diastolic pressure of spontaneously hypertensive rats at the concentration of 100 to 150 mg/kg body weight. Molecular docking simulation demonstrated that SSYYPFK could bind with the active site S1 of ACE via short hydrogen bonds. It could remain the ACE‐inhibitory activity after simulated gastrointestinal hydrolysis. Moreover, SSYYPFK showed acceptable renin and endothelin‐1 suppressing capacity (47.59% and 27.88% at 1.5 mg/mL, respectively). These results indicated that SSYYPFK may have similar antihypertensive mechanism with captopril, and could be develop to natural antihypertensive products. Practical Application One novel ACE‐inhibitory peptide SSYYPFK (890.4 Da) was identified from naked oat globulin hydrolysates. It exhibited relatively high renin and intracellular endothelin‐1 suppressing capacity, and could effectively ( P < 0.05) lower the systolic blood pressure and diastolic pressure of spontaneously hypertensive rats. This peptide could be used as natural and safe nutraceuticals and/or functional ingredients.